Two mechanisms of recovery from photoinhibition in vivo: Reactivation of photosystem II related and unrelated to D1-protein turnover

Planta ◽  
1994 ◽  
Vol 194 (1) ◽  
Author(s):  
Joachim Leitsch ◽  
Barbara Schnettger ◽  
Christa Critchley ◽  
G.Heinrich Krause
Keyword(s):  
Photosystem Ii ◽  
Protein Turnover ◽  
D1 Protein

Regulation of D1-protein degradation during photoinhibition of photosystem II in vivo: Phosphorylation of the D1 protein in various plant groups

Planta ◽  
1995 ◽  
Vol 195 (3) ◽  
Author(s):  
Eevi Rintam�ki ◽  
Riitta Salo ◽  
Elina Lehtonen ◽  
Eva-Mari Aro
Keyword(s):  
Photosystem Ii ◽  
Protein Degradation ◽  
D1 Protein ◽  
Plant Groups

scholarly journals Mechanism of REP27 Protein Action in the D1 Protein Turnover and Photosystem II Repair from Photodamage

2009 ◽  
Vol 151 (1) ◽  
pp. 88-99 ◽  
Author(s):  
David Dewez ◽  
Sungsoon Park ◽  
Jose Gines García-Cerdán ◽  
Pia Lindberg ◽  
Anastasios Melis
Keyword(s):  
Photosystem Ii ◽  
Protein Turnover ◽  
D1 Protein ◽  
Photosystem Ii Repair

Photoinactivation and recovery of photosystem II in Chenopodium album leaves grown at different levels of irradiance and nitrogen availability

2002 ◽  
Vol 29 (7) ◽  
pp. 787 ◽  
Author(s):  
Masaharu C. Kato ◽  
Kouki Hikosaka ◽  
Tadaki Hirose
Keyword(s):  
Photosystem Ii ◽  
Protein Turnover ◽  
Nitrogen Availability ◽  
Photosynthetic Capacity ◽  
Chenopodium Album ◽  
D1 Protein ◽  
High Light ◽  
High Nitrogen ◽  
Low Light ◽  
Low Nitrogen

Involvement of photosynthetic capacity and D1 protein turnover in the susceptibility of photosystem II (PSII) to photoinhibition was investigated in leaves of Chenopodium album L. grown at different combinations of irradiance and nitrogen availability: low light and high nitrogen (LL-HN); high light and low nitrogen (HL-LN); and high light and high nitrogen (HL-HN). To test the importance of photosynthetic capacity in the susceptibility to photoinhibition, we adjusted growth conditions so that HL-HN plants had the highest photosynthetic capacity, while that of LL-HN and HL-LN plants was lower but similar to each other. Photoinhibition refers here to net inactivation of PSII determined by the balance between gross inactivation (photoinactivation) and concurrent recovery of PSII via D1 protein turnover. Leaves were illuminated both in the presence and absence of lincomycin, an inhibitor of chloroplast-encoded protein synthesis. Susceptibility to photoinhibition was much higher in plants grown in low light (LL-HN) than those grown in high light (HL-HN and HL-LN). Susceptibility to photoinhibition was similar in HL-LN and HL-HN plants, suggesting that higher photosynthetic energy consumption alone did not mitigate photoinhibition. Experiments with and without lincomycin showed that high-light-grown plants had a lower rate of photoinactivation and a higher rate of concurrent recovery, and that these rates were not influenced by nitrogen availability. These results indicate that turnover of D1 protein plays a crucial role in photoprotection in high-light-grown plants, irrespective of nitrogen availability. For low-nitrogen-grown plants, higher light energy dissipation by other mechanisms may have compensated for lower energy utilization by photosynthesis.

Quality control of Photosystem II under light stress – turnover of aggregates of the D1 protein in vivo

2005 ◽  
Vol 84 (1-3) ◽  
pp. 29-33 ◽  
Author(s):  
Satoshi Ohira ◽  
Noriko Morita ◽  
Hwa-Jin Suh ◽  
Jin Jung ◽  
Yasusi Yamamoto
Keyword(s):  
Quality Control ◽  
Photosystem Ii ◽  
Light Stress ◽  
D1 Protein ◽  
Control Of Photosystem Ii

scholarly journals Structural and functional dynamics of plant photosystem II

2002 ◽  
Vol 357 (1426) ◽  
pp. 1421-1430 ◽  
Author(s):  
Jan M. Anderson ◽  
W. S. Chow
Keyword(s):  
Photosystem Ii ◽  
Singlet Oxygen ◽  
Membrane Surface ◽  
D1 Protein ◽  
Indirect Evidence ◽  
Light Level ◽  
Energy Utilization ◽  
Direct Access ◽  
Unique Problem

Given the unique problem of the extremely high potential of the oxidant P + 680 that is required to oxidize water to oxygen, the photoinactivation of photosystem II in vivo is inevitable, despite many photoprotective strategies. There is, however, a robustness of photosystem II, which depends partly on the highly dynamic compositional and structural heterogeneity of the cycle between functional and non–functional photosystem II complexes in response to light level. This coordinated regulation involves photon usage (energy utilization in photochemistry) and excess energy dissipation as heat, photoprotection by many molecular strategies, photoinactivation followed by photon damage and ultimately the D1 protein dynamics involved in the photosystem II repair cycle. Compelling, though indirect evidence suggests that the radical pair P + 680 Pheo – in functional PSII should be protected from oxygen. By analogy to the tentative oxygen channel of cytochrome c oxidase, oxygen may be liberated from the two water molecules bound to the catalytic site of the Mn cluster, via a specific pathway to the membrane surface. The function of the proposed oxygen pathway is to prevent O 2 from having direct access to P + 680 Pheo – and prevent the generation of singlet oxygen via the triplet–P 680 state in functional photosytem IIs. Only when the, as yet unidentified, potential trigger with a fateful first oxidative step destroys oxygen evolution, will the ensuing cascade of structural perturbations of photosystem II destroy the proposed oxygen, water and proton pathways. Then oxygen has direct access to P + 680 Pheo – , singlet oxygen will be produced and may successively oxidize specific amino acids of the phosphorylated D1 protein of photosystem II dimers that are confined to appressed granal domains, thereby targeting D1 protein for eventual degradation and replacement in non–appressed thylakoid domains.

Amino Acid Substitutions in the D1 Protein of Photosystem II Affect QB-Stabilization and Accelerate Turnover of D1

1990 ◽  
Vol 45 (5) ◽  
pp. 402-407 ◽  
Author(s):  
Nir Ohad ◽  
Dekel Amir-Shapira ◽  
Hiroyuki Koike ◽  
Yorinao Inoue ◽  
Itzhak Ohad ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
D1 Protein ◽  
Genetically Engineered ◽  
Close Link ◽  
Synechococcus Pcc 7942 ◽  
Temperature Downshift ◽  
The Stability ◽  
Pcc 7942 ◽  
Isogenic Strains

Abstract Isogenic strains of Synechococcus PCC 7942 were genetically engineered so that copy I of the gene psbA was mutated at specific sites. These mutations resulted in replacements of Ser 264 by Gly or Ala and of Phe 255 by Tyr or Leu in the D1 protein. The mutants were resistant to herbicides inhibiting electron transfer in photosystem II. All mutants exhibited alterations in the stability of QB- as demonstrated by a temperature downshift, to various extents, of the in vivo thermoluminescence emission. Measurements of the light-dependent turnover of D1 showed a marked decrease in the t 1/2 of this protein in the mutants as compared to wild-type, under low to medium light intensities. A correlation was found between the degree of pertur­ bation in the QB- stability and the rate of acceleration in the turnover of D1. These data pro­ vide a direct evidence for the overlapping binding sites for the plastoquinone B and herbicides in the D1 protein. In addition these data indicate a close link between QB- destabilization in reaction center II and the mechanism controlling the light-dependent turnover of D1. Based on these results and previous work we suggest that destabilization of the semireduced quinone, facilitates a light-induced damage in D1 which triggers its degradation.

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